Premium
Interaction of Lipoprotein Lipase with Heparin a
Author(s) -
OKA KAZUHIRO,
WANGIVERSON PATSY,
PATERNITI JAMES R.,
BROWN W. VIRGIL
Publication year - 1989
Publication title -
annals of the new york academy of sciences
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.712
H-Index - 248
eISSN - 1749-6632
pISSN - 0077-8923
DOI - 10.1111/j.1749-6632.1989.tb22501.x
Subject(s) - annals , library science , medicine , gerontology , classics , art , computer science
The hydrolysis of triglyceride-rich plasma lipoproteins is initiated by lipoprotein lipase (LPL) located at the luminal surface of endothelial cells. We previously reported that LPL binds to cultured endothelial cells with a Km of 2.7 x 10(-7) M and that this binding is inhibited by heparinase, heparin, or heparan sulfate. We and others recently isolated LPL cDNAs from various animals. The deduced amino acid sequence from cDNA sequence is highly conserved among animal species. The structural analysis revealed two regions rich in basic amino acid residues at the carboxyl-terminal region that may interact with the anionic heparin-like molecules. Amino acid residues 292 to 300 of bovine LPL are extremely similar to the reported heparin binding sites on apolipoproteins B-100 (amino acid residues 3359-3367) and E (amino acid residues 142-150).